Field of the Invention
The present invention relates to an Escherichia coli bacterium having an ability to produce 3-amino-4-hydroxybenzoic acid and a method for producing an amino-hydroxybenzoic acid-type compound using the same.
Brief Description of the Related Art
Amino-hydroxybenzoic acid-type compounds are useful as intermediates in the manufacture of dyes, agricultural chemicals, pharmaceuticals, and other synthesized organic products, and as a monomer of a sophisticated and heat resistant polymer, polybenzoxazole. 3-Amino-4-hydroxybenzoic acid (3,4-AHBA) is biosynthesized in two steps using the enzymes GriI and GriH. GriI catalyzes a carbon-carbon binding reaction between a C4 compound having an amino group and a C3 or C4 compound. GriH catalyzes cyclization of a C7 compound or cyclization of a C8 compound with decarboxylation. Dihydroxyacetone phosphate (DHAP) and aspartate semialdehyde (ASA) are used as substrates in the biosynthesis.

In JP 2004-283163-A, a method for producing 3,4-AHBA using Streptomyces griseus into which griI and griH were introduced is disclosed. The document also discloses that 3-acetylamino-4-hydroxybenzoic acid (3,4-AcAHBA), which is a byproduct of 3,4-AHBA, is formed and that 3,4-AcAHBA is deacetylated to form 3,4-AHBA. Use of a strong base such as sodium hydroxide and a strong acid such as hydrochloric acid is exemplified as a specific method of deacetylating 3,4-AcAHBA. However, this method has a problem that the strong base and the strong acid have to be used.
In International Publication WO2010/005099, it is disclosed that 3,4-AHBA is formed by the use of Corynebacterium glutamicum into which griI and griH were introduced.
In Suzuki et al., J. Biol. Chem., 281 (2006), 36944-36951, it is disclosed that 3,4-AHBA and 3,4-AcAHBA are formed by introducing griI and griH into Escherichia coli. 
In Suzuki et al., J. Bacteriol., 189 (2007), 2155-2159, it is disclosed that when an arylamine N-acetyltransferase gene (natA) is deleted in Streptomyces griseus, 3,4-AcAHBA is not formed in culture.
In Yamamura et al., Biochim. Biophys. Acta., 1475 (2000), 10-16, it is disclosed that an N-hydroxyarylamine O-acetyltransferase gene (nhoA) derived from Escherichia coli works to catalyze the acetylation of an aromatic amino group. Meanwhile, in Rude et al., J. Antibiot., vol. 59 (2006), p. 464, it is disclosed that Escherichia coli BAP1 strain forms an N-acetylated form (3,5-AcAHBA) as a byproduct of 3,5-AHBA (structural isomer of 3,4-AHBA). 3,5-AcAHBA is also produced as the byproduct in an nhoA gene-deleted strain (MAR1 strain) of Escherichia coli BAP1, and thus, the NhoA does not appear to be a major factor for N-acetylation of 3,5-AHBA.